Component

PTP1B preparation in the 1997 vanadate inhibition study

Context-specific entity; species, compartment and exposure are stated on each claim.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry.

    Pervanadate / peroxovanadium(V) assay species → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified PTP1B kinetic and mass-spectrometric experiments.
    limitations
    Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    The peroxide-containing species disables the enzyme through a different mechanism.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified PTP1B kinetic and mass-spectrometric experiments. · source_derived_draft · unverified_draft

    ## vanadium-pervanadate-cysteine The peroxide-containing species disables the enzyme through a different mechanism. Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry. Model: Purified PTP1B kinetic and mass-spectrometric experiments. Limitations: Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

  2. Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.

    Vanadate(V), protonation/speciation dependent → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.
    limitations
    Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 14–20

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. · source_derived_draft · unverified_draft

    ## vanadium-ptp-competitive A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery. Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar. Model: Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. Limitations: Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

  3. Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay.

    EDTA → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Enzyme assay with a vanadate-chelating reagent.
    limitations
    Biochemical reversal, not a clinical chelation treatment.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Removing available inhibitor restored activity in this preparation.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 22–28

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzyme assay with a vanadate-chelating reagent. · source_derived_draft · unverified_draft

    ## vanadium-ptp-edta-reversal Removing available inhibitor restored activity in this preparation. Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay. Model: Enzyme assay with a vanadate-chelating reagent. Limitations: Biochemical reversal, not a clinical chelation treatment. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution.

    Catalase-treated PTP1B assay → Slow time-dependent PTP1B inactivation in vanadate assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    PTP1B time-course experiments with catalase.
    limitations
    Catalase rescue supports peroxide involvement; it does not identify every species in living cells.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    An assay can generate a second inhibitor while it runs.
    primary_references
    Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 46–52

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · PTP1B time-course experiments with catalase. · source_derived_draft · unverified_draft

    ## vanadium-catalase-artifact An assay can generate a second inhibitor while it runs. Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution. Model: PTP1B time-course experiments with catalase. Limitations: Catalase rescue supports peroxide involvement; it does not identify every species in living cells. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards